Details

Autor(en) / Beteiligte

• Rietsch, Arne
• Fraisl, Peter
• Graschopf, Anton
• Bläsi, Udo

Titel

The hydrophilic C-terminal part of the lambda S holin is non-essential for intermolecular interactions

Ist Teil von

• FEMS microbiology letters, 1997-08, Vol.153 (2), p.393-398

Ort / Verlag

Oxford, UK: Blackwell Publishing Ltd

Erscheinungsjahr

1997

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• Abstract Available evidence indicates that oligomerization of the bacteriophage lambda S holin leads to a non-specific lesion in the cytoplasmic membrane which permits transit of the phage encoded transglycosylase to the periplasm. In an attempt to locate an intermolecular interaction domain in S a chimeric protein comprising the N-terminal 32 aa of phage PhiX174 lysis protein E and the last 75 aa of lambda S has been constructed. We report that the EΦS fusion protein is stable, membrane bound, and inhibits S-mediated lysis in trans. C-terminal truncations of the EΦS fusion protein indicated that the hydrophilic C-terminal end of S (i.e. the last 15 aa) is non-essential for oligomerization.